FMO2

Protein-coding gene in the species Homo sapiens
FMO2
Identifiers
AliasesFMO2, FMO1B1, flavin containing monooxygenase 2, flavin containing dimethylaniline monoxygenase 2
External IDsOMIM: 603955; MGI: 1916776; HomoloGene: 86882; GeneCards: FMO2; OMA:FMO2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for FMO2
Genomic location for FMO2
Band1q24.3Start171,185,249 bp[1]
End171,212,686 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for FMO2
Genomic location for FMO2
Band1|1 H2.1Start162,701,886 bp[2]
End162,726,295 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pericardium

  • right lung

  • lower lobe of lung

  • Descending thoracic aorta

  • lactiferous duct

  • ascending aorta

  • vena cava

  • upper lobe of lung

  • upper lobe of left lung

  • abdominal fat
Top expressed in
  • lumbar spinal ganglion

  • ascending aorta

  • right lung

  • left lung lobe

  • aortic valve

  • right lung lobe

  • pericardium

  • esophagus

  • right kidney

  • human kidney
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • oxidoreductase activity
  • N,N-dimethylaniline monooxygenase activity
  • NADP binding
  • flavin adenine dinucleotide binding
  • monooxygenase activity
Cellular component
  • organelle membrane
  • endoplasmic reticulum membrane
  • membrane
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
Biological process
  • xenobiotic metabolic process
  • toxin metabolic process
  • NADPH oxidation
  • NADP metabolic process
  • oxygen metabolic process
  • organic acid metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2327

55990

Ensembl

ENSG00000094963

ENSMUSG00000040170

UniProt

Q99518

Q8K2I3

RefSeq (mRNA)

NM_001301347
NM_001460
NM_001365900

NM_018881
NM_001360913
NM_001360914

RefSeq (protein)

NP_001288276
NP_001451
NP_001352829

NP_061369
NP_001347842
NP_001347843

Location (UCSC)Chr 1: 171.19 – 171.21 MbChr 1: 162.7 – 162.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene.[5][6][7]

The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. In most mammals, there is a flavin-containing monooxygenase that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, in humans, this enzyme is truncated and is probably rapidly degraded. The protein encoded by this gene represents the truncated form and apparently has no catalytic activity. A functional allele found in African Americans has been reported, but no sequence evidence has been deposited to support the finding. This gene is found in a cluster with the FMO1, FMO3, and FMO4 genes on chromosome 1.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000094963 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040170 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR (Nov 1992). "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family". Biochem J. 287. ( Pt 1) (Pt 1): 261–7. doi:10.1042/bj2870261. PMC 1133153. PMID 1417778.
  6. ^ Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, Phillips IR (Dec 1998). "The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein". J Biol Chem. 273 (46): 30599–607. doi:10.1074/jbc.273.46.30599. PMID 9804831.
  7. ^ a b "Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)".

Further reading

  • Hines RN, Cashman JR, Philpot RM, et al. (1994). "The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression". Toxicol. Appl. Pharmacol. 125 (1): 1–6. doi:10.1006/taap.1994.1042. PMID 8128486.
  • Lomri N, Gu Q, Cashman JR (1992). "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1685–9. Bibcode:1992PNAS...89.1685L. doi:10.1073/pnas.89.5.1685. PMC 48517. PMID 1542660.
  • Phillips IR, Dolphin CT, Clair P, et al. (1995). "The molecular biology of the flavin-containing monooxygenases of man". Chem. Biol. Interact. 96 (1): 17–32. Bibcode:1995CBI....96...17P. doi:10.1016/0009-2797(94)03580-2. PMID 7720101.
  • Lawton MP, Cashman JR, Cresteil T, et al. (1994). "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities". Arch. Biochem. Biophys. 308 (1): 254–7. doi:10.1006/abbi.1994.1035. PMID 8311461.
  • McCombie RR, Dolphin CT, Povey S, et al. (1996). "Localization of human flavin-containing monooxygenase genes FMO2 and FMO5 to chromosome 1q". Genomics. 34 (3): 426–9. doi:10.1006/geno.1996.0308. PMID 8786146.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Whetstine JR, Yueh MF, McCarver DG, et al. (2000). "Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans". Toxicol. Appl. Pharmacol. 168 (3): 216–24. doi:10.1006/taap.2000.9050. PMID 11042094.
  • Krueger SK, Martin SR, Yueh MF, et al. (2002). "Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein". Drug Metab. Dispos. 30 (1): 34–41. doi:10.1124/dmd.30.1.34. PMID 11744609. S2CID 9151632.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Furnes B, Feng J, Sommer SS, Schlenk D (2003). "Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans". Drug Metab. Dispos. 31 (2): 187–93. doi:10.1124/dmd.31.2.187. PMID 12527699. S2CID 6619389.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Krueger SK, Siddens LK, Henderson MC, et al. (2005). "Haplotype and functional analysis of four flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics". Pharmacogenet. Genomics. 15 (4): 245–56. doi:10.1097/01213011-200504000-00008. PMC 1351039. PMID 15864117.
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
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1.14.11: 2-oxoglutarate1.14.13: NADH or NADPH1.14.14: reduced flavin or flavoprotein1.14.15: reduced iron–sulfur protein1.14.16: reduced pteridine (BH4 dependent)1.14.17: reduced ascorbate1.14.18-19: other1.14.99 - miscellaneous


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